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1 sites different from those phosphorylated by pp60v-src.
2 eptor (GR) and the oncogenic tyrosine kinase pp60(v-src).
3 he N-terminal membrane-binding domain of the pp60v-src, a transforming protein whose biological activ
5 -src(527), whose respective protein products pp60v-src and pp60c-src(527) show a different spectrum o
6 eviously, p50 was observed in complexes with pp60v-src and Raf-1, but its identity and function have
7 nt step during scattering induced by HGF and pp60(v-Src) appears to be essential for cell-cell dissoc
8 ogenic protein kinases including c-raf-1 and pp60(v-src) are known to directly interact with the 90 k
17 ressed in yeast, glucocorticoid receptor and pp60(v-src) kinase, were adversely affected by cpr7 null
19 inue exploring the role of the SH2 domain in pp60v-src-mediated transformation, site-directed mutagen
20 Substrates critical for transformation by pp60v-src remain unknown, as does the precise role of th
22 -acid peptide derived from the SH2 region of pp60(v-src) tyrosine kinase, was also microinjected.